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Dithiothreitol-based protein equalisation in the context of multiple myeloma

dc.contributor.authorDomingos, Inês F.
dc.contributor.authorCarvalho, Luís B.
dc.contributor.authorLodeiro, Carlos
dc.contributor.authorGerivaz, Rita
dc.contributor.authorPrag, Gali
dc.contributor.authorMicaglio, Emanuele
dc.contributor.authorMuchtar, Eli
dc.contributor.authorSantos, Hugo M.
dc.contributor.authorCapelo, José L.
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionLAQV@REQUIMTE
dc.contributor.pblElsevier
dc.date.accessioned2024-10-09T22:41:22Z
dc.date.available2024-10-09T22:41:22Z
dc.date.issued2024-11-01
dc.descriptionPM003/ 2016). This work received support from Funda\u00E7\u00E3o para a Ci\u00EAncia e a Tecnologia and Minist\u00E9rio da Ci\u00EAncia, Tecnologia e Ensino Superior (FCT/MCTES) through the projects LA/P/0008/2020 DOI 10.54499/LA/P/0008/2020, UIDP/50006/2020 DOI 10.54499/UIDP/50006/2020 and UIDB/50006/2020 DOI 10.54499/UIDB/50006/2020. H.M.S. acknowledges the Associate Laboratory for Green Chemistry-LAQV (LA/P/0008/2020) DOI 10.54499/LA/P/0008/2020 funded by FCT/MCTES for his research contract. L.B.C. is supported by the FCT/MCTES PhD grant 2019 (SFRH/BD/144222/2019), Israel Science Foundation (ISF 1440/21) to GP. Publisher Copyright: © 2024 The Authors
dc.description.abstractIn this study, we employed the dithiothreitol-based protein equalisation technique and analytical proteomics to better understand myeloma diseases by comparing the proteomes of pellets and supernatants formed upon application of DTT on serum samples. The number of unique proteins found in pellets was 252 for healthy individuals and 223 for multiple myeloma patients. The comparison of these proteomes showed 97 dysregulated proteins. The unique proteins found for supernatants were 264 for healthy individuals and 235 for multiple myeloma patients. The comparison of these proteomes showed 87 dysregulated proteins. The analytical proteomic comparison of both groups of dysregulated proteins is translated into parallel dysregulated pathways, including chaperone-mediated autophagy and protein folding, addressing potential therapeutic interventions. Future research endeavours in personalised medicine should prioritize refining analytical proteomic methodologies using serum dithiothreitol-based protein equalisation to explore innovative therapeutic strategies. We highlight the advanced insights gained from this analytical strategy in studying multiple myeloma, emphasising its complex nature and the critical role of personalised, targeted analytical techniques in enhancing therapeutic efficacy in personalised medicine.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent8
dc.format.extent2962717
dc.identifier.doi10.1016/j.talanta.2024.126589
dc.identifier.issn0039-9140
dc.identifier.otherPURE: 98899248
dc.identifier.otherPURE UUID: a1f9c963-46d8-4b90-b8d3-b09aad08c7bc
dc.identifier.otherScopus: 85200536189
dc.identifier.otherWOS: 001293920200001
dc.identifier.otherPubMed: 39116730
dc.identifier.otherORCID: /0000-0002-6032-8679/work/170346752
dc.identifier.otherORCID: /0000-0001-5582-5446/work/201987767
dc.identifier.urihttp://hdl.handle.net/10362/173278
dc.identifier.urlhttps://www.scopus.com/pages/publications/85200536189
dc.language.isoeng
dc.peerreviewedyes
dc.relationFunding Information: PROTEOMASS Scientific Society is acknowledged by the funding provided to the Laboratory for Biological Mass Spectrometry Isabel Moura (
dc.relationPM001/2019 and
dc.subjectAmyloidosis
dc.subjectAnalytical proteomics
dc.subjectDTT equalisation
dc.subjectHaematological malignancy
dc.subjectMultiple myeloma
dc.subjectNeurotoxicity
dc.subjectProteomic profiling
dc.subjectProteostasis modulation
dc.subjectAnalytical Chemistry
dc.titleDithiothreitol-based protein equalisation in the context of multiple myelomaen
dc.title.subtitleEnhancing proteomic analysis and therapeutic insightsen
dc.typejournal article
degois.publication.titleTalanta
degois.publication.volume279
dspace.entity.typePublication
rcaap.rightsopenAccess

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